Roles of the novel coiled-coil protein Rng10 in septum formation during fission yeast cytokinesis

Liu, Yajun; Lee, I-Ju; Sun, Mingzhai; Lower, Casey A.; Runge, Kurt W.; Ma, Jianjie; Wu, Jian-Qiu

doi:10.1091/mbc.e16-03-0156

Cited by 11 publications

(34 citation statements)

References 87 publications

(147 reference statements)

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“…This may result in weakening the linkage between the strata of the contractile ring ultimately leading to loss of ring integrity and cell viability, irrespective of any mechanistic contributions of these components to ring function. In support of this hypothesis, synthetic lethality has been observed in several cases when null alleles of these genes were combined ( Ren et al, 2015 ; Pinar et al, 2008 ; Roberts-Galbraith et al, 2009 ; Liu et al, 2016 ; Chen et al, 2016 ). Indeed in the complete absence of Cdc15 and its SH3 interaction network, F-actin rings can still form but quickly disintegrate ( Laporte et al, 2011 ), underscoring the stabilizing function of the intermediate zone.…”

Section: Discussionmentioning

confidence: 86%

“…The F-BAR domain of Cdc15, also bound directly to the membrane, scaffolds the formin Cdc12 ( Willet et al, 2015b ; Carnahan and Gould, 2003 ). The membrane-binding F-BAR domain of Rga7 may also have a ring binding partner, Rng10 ( Liu et al, 2016 ), suggesting that F-BAR domains may scaffold additional ring components, linking their partners indirectly but closely to the membrane. It is not surprising that the integrity of this proximal layer of the contractile ring is critical for strong attachment to the plasma membrane.…”

Section: Discussionmentioning

confidence: 99%

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Nanoscale architecture of the Schizosaccharomyces pombe contractile ring

McDonald

Lind

Smith

et al. 2017

eLife

106

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The contractile ring is a complex molecular apparatus which physically divides many eukaryotic cells. Despite knowledge of its protein composition, the molecular architecture of the ring is not known. Here we have applied super-resolution microscopy and FRET to determine the nanoscale spatial organization of Schizosaccharomyces pombe contractile ring components relative to the plasma membrane. Similar to other membrane-tethered actin structures, we find proteins localize in specific layers relative to the membrane. The most membrane-proximal layer (0–80 nm) is composed of membrane-binding scaffolds, formin, and the tail of the essential myosin-II. An intermediate layer (80–160 nm) consists of a network of cytokinesis accessory proteins as well as multiple signaling components which influence cell division. Farthest from the membrane (160–350 nm) we find F-actin, the motor domains of myosins, and a major F-actin crosslinker. Circumferentially within the ring, multiple proteins proximal to the membrane form clusters of different sizes, while components farther from the membrane are uniformly distributed. This comprehensive organizational map provides a framework for understanding contractile ring function.

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Section: Discussionmentioning

confidence: 86%

Section: Discussionmentioning

confidence: 99%

Nanoscale architecture of the Schizosaccharomyces pombe contractile ring

McDonald

Lind

Smith

et al. 2017

eLife

106

View full text Add to dashboard Cite

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“…Superresolution microscopy PALM was performed on an inverted microscopy (IX71; Olympus, Tokyo, Japan) with a 100 ×/1.49 NA oil immersion total internal reflection fluorescence objective and an EMCCD camera (iXon Ultra 897; AndorTechnologies, Belfast, United Kingdom) with EM gain of 255 and exposure time of 0.02 s ( Liu et al. , 2016b ).…”

Section: Methodsmentioning

confidence: 99%

“…We used 405- and 488-nm diode lasers (Vortran Laser Technology, Sacramento, CA) and a 561-nm diode-pumped solid-state laser (CrystaLaser, Reno, NV) for photoactivation and imaging. Sample preparation was the same as previously described ( Liu et al. , 2016b ).…”

Section: Methodsmentioning

confidence: 99%

Roles of the fission yeast UNC-13/Munc13 protein Ync13 in late stages of cytokinesis

Zhu

Hyun

Pan

et al. 2018

MBoC

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Cytokinesis is a complicated yet conserved step of the cell-division cycle that requires the coordination of multiple proteins and cellular processes. Here we describe a previously uncharacterized protein, Ync13, and its roles during fission yeast cytokinesis. Ync13 is a member of the UNC-13/Munc13 protein family, whose animal homologues are essential priming factors for soluble N-ethylmaleimide-sensitive factor attachment protein receptor complex assembly during exocytosis in various cell types, but no roles in cytokinesis have been reported. We find that Ync13 binds to lipids in vitro and dynamically localizes to the plasma membrane at cell tips during interphase and at the division site during cytokinesis. Deletion of Ync13 leads to defective septation and exocytosis, uneven distribution of cell-wall enzymes and components of cell-wall integrity pathway along the division site and massive cell lysis during cell separation. Interestingly, loss of Ync13 compromises endocytic site selection at the division plane. Collectively, we find that Ync13 has a novel function as an UNC-13/Munc13 protein in coordinating exocytosis, endocytosis, and cell-wall integrity during fission yeast cytokinesis.

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“…In cdc15 mutants, Bgs1 trafficking from Golgi to the division site is impeded [1]. Rho-GAP Rga7 plays a role in β-1,3-glucan synthase Bgs4 delivery from Golgi to the cleavage site during cytokinesis [29,30]. The clathrin coat proteins (COPs) were also involved in glucan synthase regulation.…”

Section: Introductionmentioning

confidence: 99%

Sbg1 Is a Novel Regulator for the Localization of the β-Glucan Synthase Bgs1 in Fission Yeast

Davidson

Pontasch

2016

PLoS ONE

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Glucan synthases synthesize glucans, complex polysaccharides that are the major components in fungal cell walls and division septa. Studying regulation of glucan synthases is important as they are essential for fungal cell survival and thus popular targets for anti-fungal drugs. Linear 1,3-β-glucan is the main component of primary septum and is synthesized by the conserved β-glucan synthase Bgs1 in fission yeast cytokinesis. It is known that Rho1 GTPase regulates Bgs1 catalytic activity and the F-BAR protein Cdc15 plays a role in Bgs1 delivery to the plasma membrane. Here we characterize a novel protein Sbg1 that is present in a complex with Bgs1 and regulates its protein levels and localization. Sbg1 is essential for contractile-ring constriction and septum formation during cytokinesis. Sbg1 and Bgs1 physically interact and are interdependent for localization to the plasma membrane. Bgs1 is less stable and/or mis-targeted to vacuoles in sbg1 mutants. Moreover, Sbg1 plays an earlier and more important role in Bgs1 trafficking and localization than Cdc15. Together, our data reveal a new mode of regulation for the essential β-glucan synthase Bgs1 by the novel protein Sbg1.

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Roles of the novel coiled-coil protein Rng10 in septum formation during fission yeast cytokinesis

Cited by 11 publications

References 87 publications

Nanoscale architecture of the Schizosaccharomyces pombe contractile ring

Nanoscale architecture of the Schizosaccharomyces pombe contractile ring

Roles of the fission yeast UNC-13/Munc13 protein Ync13 in late stages of cytokinesis

Sbg1 Is a Novel Regulator for the Localization of the β-Glucan Synthase Bgs1 in Fission Yeast

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